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dc.contributor.author Pérez-Luna, Víctor H. en
dc.contributor.author Yang, Saipeng en
dc.contributor.author Rabinovich, Emmanuil M. en
dc.contributor.author Buranda, Tione en
dc.contributor.author Sklar, Larry A. en
dc.contributor.author López, Gabriel P. en
dc.contributor.author Pérez-Luna, Víctor H. en
dc.contributor.author Yang, Saipeng en
dc.contributor.author Rabinovich, Emmanuil M. en
dc.contributor.author Buranda, Tione en
dc.contributor.author Sklar, Larry A. en
dc.contributor.author López, Gabriel P. en
dc.date.accessioned 2007-01-09T20:23:14Z
dc.date.accessioned 2007-01-09T20:23:14Z
dc.date.available 2007-01-09T20:23:14Z
dc.date.available 2007-01-09T20:23:14Z
dc.date.issued 2002-01
dc.date.issued 2002-01
dc.identifier.citation Pérez-Luna, V. H., Yang S., Rabinovich, E. M., Buranda, T., Sklar, L. A., Hampton, P. D., Lopez, G. P. (2002). Fluorescence biosensing strategy based on energy transfer between fluorescently labeled receptors and a metallic surface. Biosensors and Bioelectronics v. 17 no. 1/2 p. 71-78 en
dc.identifier.citation Pérez-Luna, V. H., Yang S., Rabinovich, E. M., Buranda, T., Sklar, L. A., Hampton, P. D., Lopez, G. P. (2002). Fluorescence biosensing strategy based on energy transfer between fluorescently labeled receptors and a metallic surface. Biosensors and Bioelectronics v. 17 no. 1/2 p. 71-78 en
dc.identifier.issn 0956-5663
dc.identifier.issn 0956-5663
dc.identifier.uri doi:10.1016/S0956-5663(01)00260-3
dc.identifier.uri http://hdl.handle.net/10139/249
dc.identifier.uri doi:10.1016/S0956-5663(01)00260-3
dc.identifier.uri http://hdl.handle.net/10139/249
dc.description.abstract A new fluorescence-based biosensor is presented. The biosensing scheme is based on the fact that a fluorophore in close proximity to a metal film (<100 Å) experiences strong quenching of fluorescence and a dramatic reduction in the lifetime of the excited state. By immobilizing the analyte of interest (or a structural analog of the analyte) to a metal surface and exposing it to a labeled receptor (e.g. antibody), the fluorescence of the labeled receptor becomes quenched upon binding because of the close proximity to the metal. Upon exposure to free analyte, the labeled receptor dissociates from the surface and diffuses into the bulk of the solution. This increases its separation from the metal and an increase of fluorescence intensity and/or lifetime of the excited state is observed that indicates the presence of the soluble analyte. By enclosing this system within a small volume with a semipermeable membrane, a reversible device is obtained. We demonstrate this scheme using a biotinylated self-assembled monolayer (SAM) on gold as our surface immobilized analyte analog, fluorescently labeled anti-biotin as a receptor, and a solution of biotin in PBS as a model analyte. This scheme could easily be extended to transduce a wide variety of protein–ligand interactions and other biorecognition phenomena (e.g. DNA hybridization) that result in changes in the architecture of surface immobilized biomolecules such that a change in the separation distance between fluorophores and the metal film is obtained. en
dc.description.abstract A new fluorescence-based biosensor is presented. The biosensing scheme is based on the fact that a fluorophore in close proximity to a metal film (<100 Å) experiences strong quenching of fluorescence and a dramatic reduction in the lifetime of the excited state. By immobilizing the analyte of interest (or a structural analog of the analyte) to a metal surface and exposing it to a labeled receptor (e.g. antibody), the fluorescence of the labeled receptor becomes quenched upon binding because of the close proximity to the metal. Upon exposure to free analyte, the labeled receptor dissociates from the surface and diffuses into the bulk of the solution. This increases its separation from the metal and an increase of fluorescence intensity and/or lifetime of the excited state is observed that indicates the presence of the soluble analyte. By enclosing this system within a small volume with a semipermeable membrane, a reversible device is obtained. We demonstrate this scheme using a biotinylated self-assembled monolayer (SAM) on gold as our surface immobilized analyte analog, fluorescently labeled anti-biotin as a receptor, and a solution of biotin in PBS as a model analyte. This scheme could easily be extended to transduce a wide variety of protein–ligand interactions and other biorecognition phenomena (e.g. DNA hybridization) that result in changes in the architecture of surface immobilized biomolecules such that a change in the separation distance between fluorophores and the metal film is obtained. en
dc.description.sponsorship Office of Naval Research (N00014-95-1-1315, N00014-95-1-0901, N00014-95-1-0255), the National Science Foundation (CTS-9624841). en
dc.description.sponsorship Office of Naval Research (N00014-95-1-1315, N00014-95-1-0901, N00014-95-1-0255), the National Science Foundation (CTS-9624841). en
dc.format.extent 190958 bytes
dc.format.extent 190958 bytes
dc.format.mimetype application/pdf
dc.format.mimetype application/pdf
dc.language.iso en en
dc.language.iso en en
dc.publisher Elsevier Science B.V. en
dc.publisher Elsevier Science B.V. en
dc.rights Copyright © 2002 Elsevier Science B.V. All rights reserved. Used with permission. en
dc.rights Copyright © 2002 Elsevier Science B.V. All rights reserved. Used with permission. en
dc.subject Fluorescence en
dc.subject Lifetime en
dc.subject Energy transfer en
dc.subject Biosensor en
dc.subject Fluorescence en
dc.subject Lifetime en
dc.subject Energy transfer en
dc.subject Biosensor en
dc.title Fluorescence biosensing strategy based on energy transfer between fluorescently labeled receptors and a metallic surface en
dc.title Fluorescence biosensing strategy based on energy transfer between fluorescently labeled receptors and a metallic surface en
dc.type Postprint en
dc.type Postprint en
dc.contributor.csuciauthor Hampton, Philip D. en
dc.contributor.csuciauthor Hampton, Philip D. en


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